Magnesium in PDB 8bw9: Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp

Enzymatic activity of Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp

All present enzymatic activity of Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp:
2.7.12.2;

Other elements in 8bw9:

The structure of Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp also contains other interesting chemical elements:

Iodine (I) 1 atom
Fluorine (F) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp (pdb code 8bw9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp, PDB code: 8bw9:

Magnesium binding site 1 out of 1 in 8bw9

Go back to Magnesium Binding Sites List in 8bw9
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of the Raf Activating Complex Ksr-Mek-Cnk-Hyp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:141.8
occ:1.00
O2A C:ANP401 2.0 154.0 1.0
NZ C:LYS116 2.1 146.1 1.0
OD2 C:ASP227 2.6 112.9 1.0
CE C:LYS116 2.8 148.3 1.0
O3A C:ANP401 2.8 155.9 1.0
PA C:ANP401 3.0 156.3 1.0
C37 C:QOM402 3.8 146.0 1.0
CG C:ASP227 3.8 110.6 1.0
O5' C:ANP401 3.8 153.8 1.0
O1A C:ANP401 4.1 151.9 1.0
C35 C:QOM402 4.2 145.6 1.0
CD C:LYS116 4.2 149.1 1.0
PB C:ANP401 4.3 154.2 1.0
C36 C:QOM402 4.3 144.8 1.0
O2G C:ANP401 4.4 157.8 1.0
OD1 C:ASP227 4.4 114.5 1.0
O1B C:ANP401 4.6 149.4 1.0
CB C:ASP227 5.0 107.2 1.0

Reference:

P.Maisonneuve, S.Malha, F.Bergeron-Labrecque, M.Lefrancois, X.I.Ma, G.Arseneault, R.Fronzes, I.Kurinov, F.Sicheri, M.Therrien. The Cnk-Hyp Scaffolding Complex Promotes Raf Activation By Enhancing Ksr-Mek Interaction To Be Published 2024.
DOI: 10.1038/S41594-024-01233-6
Page generated: Thu Oct 3 19:54:43 2024

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